Synonyms

Historical Background

The dithiol-disulfide oxidoreductase protein disulfide isomerase (PDI) was discovered in 1963 as the first protein folding chaperone. Research groups led by Brunó Straub (Venetianer and Straub 1963) and Christian B. Anfinsen (Goldberger et al. 1963) independently made pivotal discoveries about an enzyme that reactivated reduced ribonuclease. Straub and coworkers purified the reactivating system from chicken pancreas. Anfinsen studied the system in conjunction with his Nobel-prize-winning work on ribonuclease and purified a system with similar activity from rat liver microsomes. In 1972, the enzyme was given the name protein disulfide isomerase and its official classification number, EC 5.3.4.1. The newly purified protein was identified as the “ribonuclease-reactivating enzyme” and was nearly identical to glutathione-insulin transhydrogenase, causing confusion in the field (Bjelland et al. 1983). Both enzymes...

Oka OBV, Yeoh HY, Bulleid NJ. Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme. Biochem J. 2015;469:279–88.PubMedPubMedCentralCrossRefGoogle Scholar